UniProt: A0A074N4F6

Database: UniProt
Entry: A0A074N4F6_9SPHN

LinkDB:  A0A074N4F6_9SPHN 
Original site:  A0A074N4F6_9SPHN

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (40)   
   InterPro (22)   
   Pfam (10)   
   PROSITE (3)   
   SMART (5)   
All databases (46)   

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ID   A0A074N4F6_9SPHN        Unreviewed;      2163 AA.
AC   A0A074N4F6;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   SubName: Full=Polyketide synthase {ECO:0000313|EMBL:KEO99073.1};
GN   ORFNames=EH32_08195 {ECO:0000313|EMBL:KEO99073.1};
OS   Erythrobacter litoralis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX   NCBI_TaxID=39960 {ECO:0000313|EMBL:KEO99073.1, ECO:0000313|Proteomes:UP000027866};
RN   [1] {ECO:0000313|EMBL:KEO99073.1, ECO:0000313|Proteomes:UP000027866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8509 {ECO:0000313|EMBL:KEO99073.1,
RC   ECO:0000313|Proteomes:UP000027866};
RA   Zheng Q.;
RT   "A comprehensive comparison of genomes of Erythrobacter spp. Strains.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KEO99073.1}.
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DR   EMBL; JMIX01000003; KEO99073.1; -; Genomic_DNA.
DR   RefSeq; WP_051697667.1; NZ_JMIX01000003.1.
DR   KEGG; elq:Ga0102493_111353; -.
DR   PATRIC; fig|39960.10.peg.431; -.
DR   OrthoDB; 9778690at2; -.
DR   Proteomes; UP000027866; Unassembled WGS sequence.
DR   GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR   Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.10.129.110; Polyketide synthase dehydratase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001227; Ac_transferase_dom_sf.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014043; Acyl_transferase.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR042104; PKS_dehydratase_sf.
DR   InterPro; IPR020807; PKS_DH.
DR   InterPro; IPR049551; PKS_DH_C.
DR   InterPro; IPR049552; PKS_DH_N.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR001031; Thioesterase.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF21089; PKS_DH_N; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   Pfam; PF14765; PS-DH; 1.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00826; PKS_DH; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027866};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          13..441
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1778..1853
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2163 AA;  235954 MW;  969D58FFBAC75F7E CRC64;
     MVDGHDDRRS GLDNRIAIVG MAAHLPGSAT LEQYWLNLRD GLECIRQYSE SELLANGEDK
     ARLLHRNYVP AAAPLDGFAD FDAGFFGLSP KEAAVMDPQH RQFLEVAWEA LETAGHPPEA
     FNGPIGVYAG CGMGSYFYFN VCSNADLVDD VGMFLLRHTG NDKDFLATRV SHVFDLKGPS
     INIQTACSTS LVAIHYACQS LLAGETDLAL AGGSTIELPQ GRGYIFQDGE ILSPDGHCHA
     FDHRAEGTVF GSGAGAVVLR RLEDALADGD HIFAVICGTA VNNDGAAKAG YLAPSVDGQS
     AAISEALDMA STPADTIDYV ECHGTGTRLG DPIEVAALTQ AFRESTEKAG FCGIGSVKTN
     IGHLDTAAGV ASTIKVALAL KNRQIPPSLG FERPNPAIDF ETSPFYVNTR LADWMATSGP
     RRAGVNSLGV GGTNAHAILE EAPEPDAHEP SDWPAQILTL SARSEAALNE ASKNLAAHLR
     SNPDQPLEDI AFTLKEGRRA FEKRRVVAVE SHAEAADRLE KGSTGRVFTH TDLGSGADVV
     FMLPGGGAQY VGMARDLYET EPVFQDAMDH GLDILDGKID YDIRALWLAE GDAAAGAGER
     LKTPSIQLPL IMITEYALAQ LWMSWGVKPT ALIGHSMGEN TAACLAGVLS FEDCLGLVHL
     RGTLFDRVPP GGMLSVPLSE ESLRAEIGDD LDVAGLNAPG LSIVSGPDEK LAELADRLAR
     REIETNRVPI NIAAHSRMLD PILPEFEAYL QSITLKPPQI PIISNRTGQP LTPEEATDPT
     YWVQHLRHTV LFADGIETLA GKRDRVYLEV GPGKALSSLA KASGKIEAQA VLTSLRHPDE
     NIADDLFFLE TLGRLWACGI QIDWGQIWGE AKRRRVPLPT YPFQRKRYFI DPADSVRPHK
     ESPLIRNEEI TEWGFVPAWL PRSAPCPVDV THELARAERH VWLVFCDSAG LGADCAARLR
     DAGHTVFEVR AGDSFLQTGD MSYTLAPERG REGYNLLLAS LVQRGITPDR IAHFWLVTRE
     EEFRPGSSFF HRNIEQGFYS LLFLAQAISE EDLPSPVSIT IVTSGAVQVR DEALLYPEKA
     IVAGPTRVIP RELPGVTCRT IDLTLPSTQR GWRRGKDEQD LREGLVPRLL EEMLAEPGNS
     DAALRDGRRY ELGIRAAPLE PVESWAQTAP EGGVWFITGG FGGIGLSVGE KLARETGAKL
     VLVSRSALPD RAQWDRALRD RPPHDKTVHR IEAVRLLEAA GAEVMVATAD VCNVSQMRTA
     IASATERFGP IHGVIHAAGA VDDAPLLTKD VSSVENVFSA KIHGTQVLDG LFPDGSVKQL
     VLFSSTSTIT APAGQIDYVA ANEYLNAYAR KRTGDATRVV AINWGIWKDV GMAAEAMAER
     QGNAPQLAPC PVDFPLLDET TFDEAGNRVF TASYTPSDRW ILDEHRTIDG TALLPGTGYI
     ELIAEALRGN GETGPFEISD LYFFSPLQVD DGTTREIRVT LIRSEEGYRV EIASDVTVDG
     RTGYHLNAQA SLALGHIPCA AQIELDAISE RMGPAERAAK NETLSSQQEA NLAFGPRWRV
     IRSMAYGHGE GLAELSLPLD FERDLKEGVV LHPALLDLAT GWAMDLIEGY DTSHLWVPVS
     YGSIRVYGPL QAELRSWVRI ATDRSEGGFA SFDVTIMDTE GQIVVEISDF SIRRLESATN
     LRSDAANLRN VVFLDQAKVK HRDLSPAEER LAHNLTQGIA PEEGAEAFRR ALGHSNAQIV
     VSSLDVQALK LQAEAQAQAD RSIGESFERP DIESDYLAPR NDIERTLAGF WQDLLGLEMV
     GVDDSFFDLG GHSLIAVRLF ALIKKTYRVE FPISVLFETP TVASIAARIA ERIGHDAHAV
     GDDDVAAEPK GRSAAVPRRF THLVPMHSGE GGQRTPFFLV AGMFGNVLNL RHLANLIGAD
     RPFYGLQARG LYGDDKPHET LSEAAADYIA EMKQIQPRGP YLVGGFSGGG LTAYEIAHQL
     EAAGEEVGLL VMLDTPLPLR PKLSTPDKVL IKLGHFREKG FGYAFKWVKA RYAWEMRRFQ
     PMEEAAAEEG LFHDKAIEAA FINALAHFDL KRWHGNLVLF RPPLDRRWKV SGDRYVSTAK
     EYVFEDNEWG QWAENLTVIE VPGDHDSMVL EPNVRVLAAE MKRCIEEAEI RSARSIEFSQ
     AAE
//

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